Evidence map›Paper›PMID 27619418›Full record

ReviewThe Journal of general physiology2016

Pore size matters for potassium channel conductance.

David Naranjo, Hans Moldenhauer, Matías Pincuntureo, Ignacio Díaz-Franulic

Open access · bronzeAbstract readReview
In one paragraph

Review in The Journal of general physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.9field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 50 citations in OpenAlex.

  1. Foldamer-based KChemical science · 2026
    Article
  2. Article
  3. Article
  4. Conduction pathway for potassium through the E. coli pump KdpFABC.bioRxiv : the preprint server for biology · 2025
    Article
  5. High-Throughput MicroED for Probing Ion Channel Dynamics.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  6. Article
  7. A new twist to increase ion flow.Nature chemical biology · 2024
    Article
  8. The Molecular Mechanism of Ion Selectivity in Nanopores.Molecules (Basel, Switzerland) · 2024
    Article
  9. Article
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. A Multi-Scale Approach to Model KFrontiers in molecular biosciences · 2022
    Article
  16. Selectivity filter modalities and rapid inactivation of the hERG1 channel.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  17. Article
  18. Review
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 1 country.

David NaranjoCentro Interdisciplinario de Neurociencia de Valparaíso, Universidad de Valparaíso, Playa Ancha, Valparaíso 2360103, Chile david.naranjo@uv.cl ignacio.diaz@cinv.cl.ORCID 0000-0003-3482-5126
Hans MoldenhauerCentro Interdisciplinario de Neurociencia de Valparaíso, Universidad de Valparaíso, Playa Ancha, Valparaíso 2360103, Chile.
Matías PincuntureoCentro Interdisciplinario de Neurociencia de Valparaíso, Universidad de Valparaíso, Playa Ancha, Valparaíso 2360103, Chile Programa de Doctorado en Ciencias, mención Biofísica y Biología Computacional, Universidad de Valparaíso, Valparaíso 2360103, Chile.
Ignacio Díaz-FranulicCentro Interdisciplinario de Neurociencia de Valparaíso, Universidad de Valparaíso, Playa Ancha, Valparaíso 2360103, Chile Center for Bioinformatics and Integrative Biology, Universidad Andrés Bello, Santiago 8370146, Chile Fraunhofer Chile Research, Las Condes 7550296, Chile david.naranjo@uv.cl ignacio.diaz@cinv.cl.
University of Valparaíso · CLUniversidad Andrés Bello · CLUniversidad de Playa Ancha de Ciencias de la Educación · CL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ion channels are membrane proteins that mediate efficient ion transport across the hydrophobic core of cell membranes, an unlikely process in their absence. K(+) channels discriminate K(+) over cations with similar radii with extraordinary selectivity and display a wide diversity of ion transport rates, covering differences of two orders of magnitude in unitary conductance. The pore domains of large- and small-conductance K(+) channels share a general architectural design comprising a conserved narrow selectivity filter, which forms intimate interactions with permeant ions, flanked by two wider vestibules toward the internal and external openings. In large-conductance K(+) channels, the inner vestibule is wide, whereas in small-conductance channels it is narrow. Here we raise the idea that the physical dimensions of the hydrophobic internal vestibule limit ion transport in K(+) channels, accounting for their diversity in unitary conductance.

Indexed as

Ion TransportModels, MolecularPotassiumPotassium ChannelsProtein ConformationPotassiumPotassium Channels

Identifiers

PMID27619418
PMCPMC5037345
OpenAlexW2518880905

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.